 A new drug is developed which selectively cleaves covalent

bonds between two sulfur atoms of non-adjacent amino acids
in a polypeptide chain. Which level of protein structure in
affected molecules would be most directly affected by the
drug

3 answers

The tertiary structure of the affected protein molecules would be most directly affected by the drug as it is the level of protein structure where the non-adjacent amino acids are held together by disulfide bonds formed between the sulfur atoms. Disrupting these bonds would cause a structural change in the protein, altering its function.
Albumin is a large protein which circulates freely in human plasma. Another
type of protein, called aquaporins, act as a channel for water to enter and exit a
cell, and are located within the lipid bilayer of a cell’s plasma membrane. Based
on their physiological locations, how would the tertiary structure of these two
proteins mostly likely compare?
a. Albumin has more of nonpolar core with nonpolar out layer while
aquaporins have a more polar core with polar outer layer.
b. Albumin has more of nonpolar core with polar outer later while
aquaporins have more polar core with nonpolar outer layer.
c. Albumin has more polar core with non polar outer layer while
aquaporins have a more of non polar core with polar outer layer
d. Albumin has more polar core with polar outer layer while aquaporins
have a more of non polar core with non polar outer layer
c. Albumin has more polar core with non polar outer layer while aquaporins have a more non polar core with polar outer layer.

Albumin is a soluble protein that circulates freely in blood plasma, so it needs to be water-soluble. Therefore, it has a polar (hydrophilic) core that can interact with water molecules and a non-polar (hydrophobic) outer layer that interacts with other non-polar molecules in the body.

Aquaporins, on the other hand, are membrane proteins that need to interact with the non-polar lipid bilayer of the cell membrane in order to function. Therefore, they have a non-polar (hydrophobic) core that can interact with the lipid bilayer and a polar (hydrophilic) outer layer that interacts with water molecules.